Source:http://linkedlifedata.com/resource/pubmed/id/18007056
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 11
|
pubmed:dateCreated |
2007-11-16
|
pubmed:abstractText |
The flavin-dependent monooxygenase RebC is a key enzyme in the biosynthesis of the indolocarbazole rebeccamycin. The synthesis of rebeccamycin is of great interest as it has been shown to be a natural antitumour agent. The enzyme has been recombinantly expressed in Escherichia coli and purified to homogeneity. Hanging-drop vapour diffusion in combination with microseeding was used to obtain suitable crystals for X-ray diffraction. Data were collected to 2.4 A; the crystals belonged to space group P2(1), with unit-cell parameters a = 63.08, b = 77.85, c = 63.94 A, alpha = gamma = 90, beta = 108.11 degrees .
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007056-12619684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007056-15625109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007056-16967980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007056-17705392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007056-3112080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007056-5700707
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
1744-3091
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
1
|
pubmed:volume |
63
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
980-2
|
pubmed:dateRevised |
2010-9-14
|
pubmed:meshHeading | |
pubmed:year |
2007
|
pubmed:articleTitle |
Expression, purification and preliminary X-ray diffraction studies of RebC.
|
pubmed:affiliation |
Department of Biochemistry, Queen's University, Kingston K7L 3N6, Canada.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|